应用天然产物 ›› 2014, Vol. 4 ›› Issue (5): 309-313.DOI: 10.1007/s13659-014-0037-z
• Original article • 上一篇
Guo-Xiang Mo1, Xue-Wei Bai1, Zong-Jie Li1, Xiu-Wen Yan1, Xiao-Qing He2, Ming-Qiang Rong2
Guo-Xiang Mo1, Xue-Wei Bai1, Zong-Jie Li1, Xiu-Wen Yan1, Xiao-Qing He2, Ming-Qiang Rong2
摘要: Various kinds of biologically active peptides have previously been isolated from the skin secretions of Amolops loloensis frog, such as antimicrobial peptides, bradykinin-like peptides and algesic peptides. A novel insulinotropic peptide named amolopin was identified in A. loloensis frog's skin secretion. Its primary structure sequence was determined by Edman degradation as: FLPIVGKSLSGLSGKL-NH2. BLAST search indicates that the amino acid sequence of amolopin is quite different from other known insulin secretagogues, including mastoparan, exendins and a-latrotoxin, nor does it like incretins(e.g. glucagons like peptide-1 and glucose-dependent insulinotropic ploypeptide) either. However, amolopin shows certain structural similarity with amphibian antimicrobial temporins and vespid chemotactic peptides isolated from Vespa magnifica. Amolopin can stimulate insulin release in INS-1 cells in a dose-dependent manner. Primary investigation on its action mechanisms reveals that amolopin does not increase the influx of Ca2+. In conclusion, a novel 16-amino acid peptide with insulin-releasing activity is initially discovered from the skin secretion of A. loloensis frog. Further work is necessary to evaluate its potential as novel anti-diabetic candidate.